Author: Nobili, A.; Steffen-Munsberg, F.; Kohls, H.; Trentin, I.; Schulzke, C.; Höhne, M.; Bornscheuer, U.T.
Description: Although the amine transaminase from Vibrio fluvialis has often been applied as a catalyst for the biocatalytic preparation of various chiral primary amines, it is not suitable for the transamination of alpha-hydroxy ketones and aryl-alkyl ketones bearing an alkyl substituent larger than a methyl group. We addressed this problem through a systematic mutagenesis study of active site residues to expand its substrate scope towards two bulky ketones. We identified two mutants (F85L/V153A and Y150F/V153A) showing 30-fold increased activity in the conversion of (S)-phenylbutylamine and (R)-phenylglycinol, respectively. Notably, they facilitated asymmetric synthesis of these amines with excellent enantiomeric purities of 98% ee.
Subject headings: Amine Transaminase; Synthesis; Aryl-Alkyl Amines; Amino Alcohols; Vibrio fluvialis
Publication year: 2015
Journal or book title: ChemCatChem
Volume: 7
Issue: 5
Pages: 757-760
Find the full text : https://chemistry-europe.onlinelibrary.wiley.com/doi/abs/10.1002/cctc.201403010
Find more like this one (cited by): https://scholar.google.com/scholar?cites=9122505675399183168&as_sdt=1000005&sciodt=0,16&hl=en
Type: Journal Article
Serial number: 2355